Research workbench
Cryo-EM structures of aerolysin post-prepore and quasipore
Analyse Cryo-EM structures of aerolysin post-prepore and quasipore in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JZW
- Type
- protein
- Length
- 5,474 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aerolysin
- UniProt
- P09167
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 17% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Aerolysin | protein | 381 | 16% helix, 33% strand | P09167 |
| H, I, J, K, L, M, N | Aerolysin | protein | 401 | 17% helix, 36% strand | P09167 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1082 | 0.84 | 0.85 | 140 | empty |
| 2 | 1082 | 0.84 | 0.85 | 131 | empty |
| 3 | 873 | 0.78 | 0.80 | 83 | empty |
| 4 | 870 | 0.77 | 0.80 | 92 | empty |
| 5 | 1001 | 0.76 | 0.79 | 104 | empty |
Interfaces
35 interfaces between chains.
- H–I · 3148 Ų buried · 66 hydrogen bonds · protein-protein
- H–N · 3145 Ų buried · 66 hydrogen bonds · protein-protein
- J–K · 3144 Ų buried · 66 hydrogen bonds · protein-protein
- I–J · 3144 Ų buried · 66 hydrogen bonds · protein-protein
- M–N · 3142 Ų buried · 66 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 28 disulfide (disulfide).
Compared structures
- 5JZW · Cryo-EM structures of aerolysin post-prepore and quasipore · the same entry in another collection · chain I against I, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P09167
- Elsewhere: RCSB PDB 5JZW · PDBe 5JZW · UniProt P09167
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